| Online-Ressource |
Verfasst von: | Tempra, Carmelo [VerfasserIn]  |
| Scollo, Federica [VerfasserIn]  |
| Pannuzzo, Martina [VerfasserIn]  |
| Lolicato, Fabio [VerfasserIn]  |
| La Rosa, Carmelo [VerfasserIn]  |
Titel: | A unifying framework for amyloid-mediated membrane damage |
Titelzusatz: | the lipid-chaperone hypothesis |
Verf.angabe: | Carmelo Tempra, Federica Scollo, Martina Pannuzzo, Fabio Lolicato, Carmelo La Rosa |
E-Jahr: | 2022 |
Jahr: | 8 February 2022 |
Umfang: | 13 S. |
Fussnoten: | Gesehen am 30.08.2022 |
Titel Quelle: | Enthalten in: Biochimica et biophysica acta / Proteins and proteomics |
Ort Quelle: | Amsterdam [u.a.], 2002 |
Jahr Quelle: | 2022 |
Band/Heft Quelle: | 1870(2022), 4, Artikel-ID 140767, Seite 1-13 |
ISSN Quelle: | 1878-1454 |
Abstract: | Over the past thirty years, researchers have highlighted the role played by a class of proteins or polypeptides that forms pathogenic amyloid aggregates in vivo, including i) the amyloid Aβ peptide, which is known to form senile plaques in Alzheimer's disease; ii) α-synuclein, responsible for Lewy body formation in Parkinson's disease and iii) IAPP, which is the protein component of type 2 diabetes-associated islet amyloids. These proteins, known as intrinsically disordered proteins (IDPs), are present as highly dynamic conformational ensembles. IDPs can partially (mis) fold into (dys) functional conformations and accumulate as amyloid aggregates upon interaction with other cytosolic partners such as proteins or lipid membranes. In addition, an increasing number of reports link the toxicity of amyloid proteins to their harmful effects on membrane integrity. Still, the molecular mechanism underlying the amyloidogenic proteins transfer from the aqueous environment to the hydrocarbon core of the membrane is poorly understood. This review starts with a historical overview of the toxicity models of amyloidogenic proteins to contextualize the more recent lipid-chaperone hypothesis. Then, we report the early molecular-level events in the aggregation and ion-channel pore formation of Aβ, IAPP, and α-synuclein interacting with model membranes, emphasizing the complexity of these processes due to their different spatial-temporal resolutions. Next, we underline the need for a combined experimental and computational approach, focusing on the strengths and weaknesses of the most commonly used techniques. Finally, the last two chapters highlight the crucial role of lipid-protein complexes as molecular switches among ion-channel-like formation, detergent-like, and fibril formation mechanisms and their implication in fighting amyloidogenic diseases. |
DOI: | doi:10.1016/j.bbapap.2022.140767 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.1016/j.bbapap.2022.140767 |
| DOI: https://doi.org/10.1016/j.bbapap.2022.140767 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | Aggregation |
| alpha-Synuclein |
| Amyloid |
| Amyloidogenic Proteins |
| Amyloidosis |
| Diabetes Mellitus, Type 2 |
| Humans |
| Intrinsically Disordered Proteins |
| Ion channel-like |
| Lipid-chaperone |
| Lipids |
| Model membrane |
| Molecular Chaperones |
| Peptides |
| Toxic oligomer |
K10plus-PPN: | 1815384085 |
Verknüpfungen: | → Zeitschrift |
¬A¬ unifying framework for amyloid-mediated membrane damage / Tempra, Carmelo [VerfasserIn]; 8 February 2022 (Online-Ressource)